REFERENCES


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Very N, Hardivillé S, Decourcelle A, Thévenet J, Djouina M, Page A, Vergoten G, Schulz C, Kerr-Conte J, Lefebvre T, Dehennaut V, El Yazidi-Belkoura I. Thymidylate synthase O-GlcNAcylation: a molecular mechanism of 5-FU sensitization in colorectal cancer. Oncogene 2022 41(5) 34845374
Abstract:
Alteration of O-GlcNAcylation, a dynamic posttranslational modification, is associated with tumorigenesis and tumor progression. Its role in chemotherapy response is poorly investigated. Standard treatment for colorectal cancer (CRC), 5-fluorouracil (5-FU), mainly targets Thymidylate Synthase (TS). TS O-GlcNAcylation was reported but not investigated yet. We hypothesize that O-GlcNAcylation interferes with 5-FU CRC sensitivity by regulating TS. In vivo, we observed that combined 5-FU with Thiamet-G (O-GlcNAcase (OGA) inhibitor) treatment had a synergistic inhibitory effect on grade and tumor progression. 5-FU decreased O-GlcNAcylation and, reciprocally, elevation of O-GlcNAcylation was associated with TS increase. In vitro in non-cancerous and cancerous colon cells, we showed that 5-FU impacts O-GlcNAcylation by decreasing O-GlcNAc Transferase (OGT) expression both at mRNA and protein levels. Reciprocally, OGT knockdown decreased 5-FU-induced cancer cell apoptosis by reducing TS protein level and activity. Mass spectrometry, mutagenesis and structural studies mapped O-GlcNAcylated sites on T251 and T306 residues and deciphered their role in TS proteasomal degradation. We reveal a crosstalk between O-GlcNAcylation and 5-FU metabolism in vitro and in vivo that converges to 5-FU CRC sensitization by stabilizing TS. Overall, our data propose that combining 5-FU-based chemotherapy with Thiamet-G could be a new way to enhance CRC response to 5-FU.
O-GlcNAc proteins:
TYSY
Species: Homo sapiens
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Kasprowicz A, Spriet C, Terryn C, Rigolot V, Hardiville S, Alteen MG, Lefebvre T, Biot C. Exploring the Potential of β-Catenin O-GlcNAcylation by Using Fluorescence-Based Engineering and Imaging. Molecules (Basel, Switzerland) 2020 25(19) 33019562
Abstract:
Monitoring glycosylation changes within cells upon response to stimuli remains challenging because of the complexity of this large family of post-translational modifications (PTMs). We developed an original tool, enabling labeling and visualization of the cell cycle key-regulator β-catenin in its O-GlcNAcylated form, based on intramolecular Förster resonance energy transfer (FRET) technology in cells. We opted for a bioorthogonal chemical reporter strategy based on the dual-labeling of β-catenin with a green fluorescent protein (GFP) for protein sequence combined with a chemically-clicked imaging probe for PTM, resulting in a fast and easy to monitor qualitative FRET assay. We validated this technology by imaging the O-GlcNAcylation status of β-catenin in HeLa cells. The changes in O-GlcNAcylation of β-catenin were varied by perturbing global cellular O-GlcNAc levels with the inhibitors of O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA). Finally, we provided a flowchart demonstrating how this technology is transposable to any kind of glycosylation.
O-GlcNAc proteins:
CTNB1
Species: Homo sapiens
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Masclef L, Dehennaut V, Mortuaire M, Schulz C, Leturcq M, Lefebvre T, Vercoutter-Edouart AS. Cyclin D1 Stability Is Partly Controlled by O-GlcNAcylation. Frontiers in endocrinology 2019 10 30853938
Abstract:
Cyclin D1 is the regulatory partner of the cyclin-dependent kinases (CDKs) CDK4 or CDK6. Once associated and activated, the cyclin D1/CDK complexes drive the cell cycle entry and G1 phase progression in response to extracellular signals. To ensure their timely and accurate activation during cell cycle progression, cyclin D1 turnover is finely controlled by phosphorylation and ubiquitination. Here we show that the dynamic and reversible O-linked β-N-Acetyl-glucosaminylation (O-GlcNAcylation) regulates also cyclin D1 half-life. High O-GlcNAc levels increase the stability of cyclin D1, while reduction of O-GlcNAcylation strongly decreases it. Moreover, elevation of O-GlcNAc levels through O-GlcNAcase (OGA) inhibition significantly slows down the ubiquitination of cyclin D1. Finally, biochemical and cell imaging experiments in human cancer cells reveal that the O-GlcNAc transferase (OGT) binds to and glycosylates cyclin D1. We conclude that O-GlcNAcylation promotes the stability of cyclin D1 through modulating its ubiquitination.
O-GlcNAc proteins:
CCND1
Species: Homo sapiens
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Biwi J, Clarisse C, Biot C, Kozak RP, Madunic K, Mortuaire M, Wuhrer M, Spencer DIR, Schulz C, Guerardel Y, Lefebvre T, Vercoutter-Edouart AS. OGT Controls the Expression and the Glycosylation of E-cadherin, and Affects Glycosphingolipid Structures in Human Colon Cell Lines. Proteomics 2019 19(21-22) 31373757
Abstract:
Colorectal cancer (CRC) affects both women and men living in societies with a high sedentary lifestyle. Amongst the phenotypic changes exhibited by tumor cells, a wide range of glycosylation has been reported for colon cancer-derived cell lines and CRC tissues. These aberrant modifications affect different aspects of glycosylation, including an increase in core fucosylation and GlcNAc branching on N-glycans, alteration of O-glycans, upregulated sialylation, and O-GlcNAcylation. Although O-GlcNAcylation and complex glycosylations differ in many aspects, sparse evidences report on the interference of O-GlcNAcylation with complex glycosylation. Nevertheless, this relationship is still a matter of debate. Combining different approaches on three human colon cell lines (HT29, HCT116 and CCD841CoN), it is herein reported that silencing O-GlcNAc transferase (OGT, the sole enzyme driving O-GlcNAcylation), only slightly affects overall N- and O-glycosylation patterns. Interestingly, silencing of OGT in HT29 cells upregulates E-cadherin (a major actor of epithelial-to-mesenchymal transition) and changes its glycosylation. On the other hand, OGT silencing perturbs biosynthesis of glycosphingolipids resulting in a decrease in gangliosides and an increase in globosides. Together, these results provide novel insights regarding the selective regulation of complex glycosylations by O-GlcNAcylation in colon cancer cells.
O-GlcNAc proteins:
CADH1
Species: Homo sapiens
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Torres-Gutiérrez E, Pérez-Cervera Y, Camoin L, Zenteno E, Aquino-Gil MO, Lefebvre T, Cabrera-Bravo M, Reynoso-Ducoing O, Bucio-Torres MI, Salazar-Schettino PM. Identification of O-Glcnacylated Proteins in Trypanosoma cruzi. Frontiers in endocrinology 2019 10 30984116
Abstract:
Originally an anthropozoonosis in the Americas, Chagas disease has spread from its previous borders through migration. It is caused by the protozoan Trypanosoma cruzi. Differences in disease severity have been attributed to a natural pleomorphism in T. cruzi. Several post-translational modifications (PTMs) have been studied in T. cruzi, but to date no work has focused on O-GlcNAcylation, a highly conserved monosaccharide-PTM of serine and threonine residues mainly found in nucleus, cytoplasm, and mitochondrion proteins. O-GlcNAcylation is thought to regulate protein function analogously to protein phosphorylation; indeed, crosstalk between both PTMs allows the cell to regulate its functions in response to nutrient levels and stress. Herein, we demonstrate O-GlcNAcylation in T. cruzi epimastigotes by three methods: by using specific antibodies against the modification in lysates and whole parasites, by click chemistry labeling, and by proteomics. In total, 1,271 putative O-GlcNAcylated proteins and six modification sequences were identified by mass spectrometry (data available via ProteomeXchange, ID PXD010285). Most of these proteins have structural and metabolic functions that are essential for parasite survival and evolution. Furthermore, O-GlcNAcylation pattern variations were observed by antibody detection under glucose deprivation and heat stress conditions, supporting their possible role in the adaptive response. Given the numerous biological processes in which O-GlcNAcylated proteins participate, its identification in T. cruzi proteins opens a new research field in the biology of Trypanosomatids, improve our understanding of infection processes and may allow us to identify new therapeutic targets.
O-GlcNAc proteins:
A0A0F6YF08, A0A0M3NVD0, A0A0M3YBC4, A0A189XHE2, A0A1B1R0W9, A0A286R981, A0SZK3, A5JUX3, A6N830, A7UL80, B3U4H3, B5U6U4, C9DS87, D1LWU5, D9I8N9, G0Z187, G4WJW3, G8FL60, H9AZG3, H9AZH1, H9AZH6, H9M3L8, I3QF27, J3JZZ0, K2LUZ2, K2LV71, K2LVR5, K2LVZ1, K2LXG1, K2LY59, K2LY67, K2LYT1, K2LZ01, K2M094, K2M439, K2M491, K2M4M1, K2M4S3, K2M518, K2M526, K2M5Q0, K2M5Q3, K2M5W0, K2M603, K2M6U1, K2M6U4, K2M741, K2M7F4, K2M7Z5, K2M842, K2M892, K2M9C4, K2M9U9, K2MA70, K2MAF9, K2MAY5, K2MAZ3, K2MCN3, K2MCT5, K2MCY1, K2MDE9, K2MDJ7, K2MEB2, K2MHI4, K2MI51, K2MK39, K2MKM4, K2MKU0, K2MLW4, K2MM88, K2MN29, K2MN89, K2MNC2, K2MNF2, K2MNK2, K2MNZ2, K2MPW1, K2MQ45, K2MQ55, K2MQY7, K2MR15, K2MRQ3, K2MRY2, K2MSQ3, K2MSW9, K2MT40, K2MTF7, K2MTH2, K2MU46, K2MUF1, K2MUS2, K2MVC2, K2MVK4, K2MVP9, K2MVW9, K2MVZ1, K2MW43, K2MW55, K2MWA1, K2MWQ0, K2MWX3, K2MWY1, K2MX11, K2MXC9, K2MXG0, K2MXN7, K2MXT6, K2MXY3, K2MY44, K2MY82, K2MYH5, K2MYY2, K2MZ11, K2MZF4, K2MZF5, K2MZJ0, K2MZL9, K2N002, K2N008, K2N040, K2N084, K2N0A2, K2N0N5, K2N0W4, K2N128, K2N161, K2N1L0, K2N1M9, K2N200, K2N232, K2N279, K2N4P9, K2N598, K2N5B4, K2N5L9, K2N5P8, K2N5S2, K2N5W3, K2N683, K2N687, K2N6G2, K2N6M0, K2N6V1, K2N704, K2N8E5, K2N987, K2N9B5, K2NA63, K2NAE4, K2NAH8, K2NBJ9, K2NBK1, K2NC20, K2NC76, K2NC82, K2NC88, K2NCV2, K2NE71, K2NE72, K2NE80, K2NES1, K2NEY2, K2NFF1, K2NG18, K2NGH9, K2NGI2, K2NGT6, K2NH93, K2NHB5, K2NIQ0, K2NJ61, K2NJG1, K2NJM5, K2NJP3, K2NJP7, K2NL34, K2NLA3, K2NLJ5, K2NLK6, K2NLQ2, K2NMM5, K2NNM1, K2NP04, K2NP31, K2NQC5, K2NRA3, K2NSB8, K2NSH4, K2NSL2, K2NSP8, K2NSS5, K2NTN6, K2NVY6, K2NW21, K2NW49, K2NW93, K2NWK7, K2NX50, K2P6Y7, K2P9C9, K2PAY9, K2PBQ1, K2PCH2, K2PCJ0, K2PDG2, K2PDY3, K2PE13, K2PFE2, K4E123, K7SWG8, K7ZR76, M4H1F5, M4H1T0, M4H2K1, RL28, O15637, O60947, O60996, O61066, O61083, O61084, O62594, O76138, O77252, O79469, O96673, TCP17, HSP70, HSP85, RL402, G3PG, TCNA, RLA1, ATTY, TPIS, PSA1, Q003G7, Q1WBU6, Q26858, Q26887, Q26936, Q26944, Q26947, Q26952, Q27791, Q27796, Q2I5R9, Q2TJ65, Q3ZMB7, Q49UB9, Q4CKT7, Q4CLI0, Q4CLM5, Q4CLN1, Q4CLP6, Q4CLQ9, Q4CLR4, Q4CLV8, Q4CLW3, Q4CLY6, Q4CM27, Q4CM56, Q4CM68, Q4CM72, Q4CM73, Q4CMA6, Q4CME2, Q4CMM4, Q4CMR1, Q4CMS5, Q4CMT2, Q4CMU8, Q4CN66, Q4CN82, Q4CNC6, Q4CNF4, Q4CNM5, Q4CNU0, Q4CP05, Q4CP06, Q4CP28, Q4CP43, Q4CP89, Q4CP97, Q4CPE2, Q4CPG3, Q4CPG4, Q4CPJ3, Q4CPK3, Q4CPK8, Q4CPM5, Q4CPP0, Q4CPR5, Q4CPU3, Q4CPV9, Q4CPW5, Q4CQ34, Q4CQ46, Q4CQ54, Q4CQ63, Q4CQ81, Q4CQA1, Q4CQG0, Q4CQI9, Q4CQM4, Q4CQR0, Q4CQX2, Q4CR06, Q4CR09, Q4CR35, Q4CR84, Q4CRA7, Q4CRH9, Q4CRK6, Q4CRM4, Q4CRM5, Q4CRN7, Q4CRN8, Q4CRQ6, Q4CRR1, Q4CRT0, Q4CRU8, Q4CRX5, Q4CS11, Q4CS16, Q4CS20, Q4CS26, Q4CS27, Q4CS80, Q4CS87, Q4CSD4, Q4CSD9, Q4CSI4, Q4CSI8, Q4CSK3, Q4CSK4, Q4CSL1, Q4CSL9, Q4CSN9, Q4CSR6, Q4CSR8, Q4CSV9, Q4CSY5, Q4CT37, Q4CTC0, Q4CTD7, Q4CTE7, Q4CTG8, Q4CTK4, Q4CTP1, Q4CTS3, Q4CTS4, Q4CTV7, Q4CU52, Q4CU59, Q4CU61, Q4CU72, Q4CU74, Q4CU77, Q4CU84, Q4CU91, Q4CU92, Q4CUC8, Q4CUE0, Q4CUF9, Q4CUL1, Q4CUV9, Q4CUW8, Q4CUZ7, Q4CV48, Q4CV87, Q4CVC6, Q4CVE1, Q4CVG3, Q4CVJ1, Q4CVJ2, Q4CVJ7, Q4CVL1, Q4CVP1, Q4CVQ3, Q4CVR9, Q4CVT7, Q4CVW3, Q4CVX7, Q4CVX9, Q4CW02, Q4CW22, Q4CW23, Q4CW28, Q4CW30, Q4CW52, Q4CW64, Q4CWE3, Q4CWE6, Q4CWM5, Q4CWM6, Q4CWN9, Q4CWQ8, Q4CWR1, Q4CWT2, Q4CWY3, Q4CX80, Q4CXC3, Q4CXE1, Q4CXE8, Q4CXI6, Q4CXJ4, Q4CXJ6, Q4CXJ7, Q4CXK2, Q4CXN4, Q4CXN8, Q4CXQ1, Q4CXR7, Q4CXR9, Q4CXV1, Q4CXW2, Q4CXW9, Q4CXX9, Q4CY01, Q4CY08, Q4CY21, Q4CY42, Q4CY95, Q4CYA5, Q4CYC6, Q4CYE2, Q4CYE8, Q4CYG8, Q4CYH9, Q4CYL3, Q4CYN4, Q4CYN6, Q4CYR3, Q4CYW6, Q4CYZ1, Q4CYZ6, Q4CZ11, Q4CZ35, Q4CZB7, Q4CZF0, Q4CZF4, Q4CZG5, Q4CZK3, Q4CZK9, Q4CZQ3, Q4CZQ7, Q4CZR0, Q4CZT6, Q4CZV4, Q4CZX4, Q4CZY1, Q4CZZ3, Q4D049, Q4D059, Q4D066, Q4D078, Q4D083, Q4D085, Q4D0A7, Q4D0A9, Q4D0C0, Q4D0E4, Q4D0K8, Q4D0M6, Q4D0R4, Q4D0S6, Q4D0U5, Q4D0W7, Q4D0X1, Q4D139, Q4D144, Q4D157, Q4D189, Q4D193, Q4D1D3, Q4D1I7, Q4D1P9, Q4D1Q4, Q4D1R0, Q4D1V7, Q4D1Y5, Q4D1Y7, Q4D205, Q4D214, Q4D276, Q4D2D7, Q4D2I4, Q4D2R8, RS3A1, Q4D2T0, Q4D2X1, Q4D2Z8, Q4D3A9, DRE21, Q4D3E3, Q4D3H6, Q4D3T1, Q4D3V3, PYRD, Q4D3W7, Q4D425, Q4D436, Q4D487, Q4D4E6, Q4D4F5, Q4D4L3, Q4D4M0, Q4D4M2, Q4D4N6, Q4D4R0, Q4D4R9, Q4D4S1, Q4D4V5, Q4D4X1, Q4D4X6, ECOT2, Q4D4Y8, Q4D4Z3, Q4D518, Q4D528, Q4D546, Q4D578, Q4D579, Q4D588, Q4D590, Q4D5C1, Q4D5E8, Q4D5R2, Q4D5T6, Q4D5V2, Q4D5X2, Q4D5Z3, Q4D630, Q4D6D8, Q4D6F1, Q4D6H3, Q4D6I3, Q4D6I5, Q4D6J0, Q4D6M9, Q4D6N5, Q4D6P0, Q4D6P2, Q4D6Q6, Q4D6V2, Q4D6Z3, Q4D722, Q4D747, Q4D751, Q4D758, Q4D779, Q4D795, Q4D7A0, Q4D7D2, Q4D7D9, Q4D7G9, Q4D7L3, Q4D7P6, Q4D7T7, Q4D7X5, Q4D820, Q4D823, Q4D864, Q4D866, Q4D867, Q4D8B1, Q4D8D3, Q4D8D7, Q4D8J9, Q4D8K3, Q4D8S5, Q4D8U0, Q4D930, Q4D966, Q4D968, Q4D9B4, Q4D9F7, Q4D9H3, Q4D9L7, Q4D9M6, Q4D9P7, Q4D9Q4, Q4D9Q8, Q4D9Q9, Q4D9S6, Q4D9S8, Q4D9Z1, Q4D9Z2, Q4D9Z9, Q4DA08, Q4DA32, Q4DA33, Q4DA54, Q4DA86, Q4DAD2, Q4DAE1, Q4DAF0, Q4DAG5, Q4DAK5, Q4DAN2, Q4DAP4, Q4DAU6, Q4DAV0, Q4DAV1, Q4DAX6, Q4DAY6, Q4DAZ6, Q4DB19, Q4DB46, Q4DB81, Q4DBB6, Q4DBC5, Q4DBG8, Q4DBH3, Q4DBL6, Q4DBP4, Q4DBR1, Q4DBS8, Q4DBV1, Q4DBY3, Q4DC00, Q4DC38, Q4DC65, Q4DCA9, Q4DCC6, Q4DCH7, Q4DCI2, Q4DCI5, Q4DCL6, Q4DCM3, Q4DCN7, Q4DCQ5, Q4DCV7, Q4DCX1, Q4DCY3, Q4DD18, Q4DD50, Q4DD81, Q4DDC1, Q4DDH1, Q4DDI3, Q4DDI8, Q4DDK6, Q4DDL0, Q4DDN8, Q4DDP3, Q4DDS8, Q4DDT6, Q4DDW5, Q4DDZ3, Q4DE00, Q4DE24, Q4DE31, Q4DE50, Q4DE52, Q4DE75, Q4DE88, Q4DEA8, Q4DEC1, Q4DEC2, Q4DED2, Q4DED3, Q4DEE6, Q4DEE8, Q4DEI2, Q4DEJ1, Q4DEJ6, Q4DEM5, Q4DER7, Q4DES9, Q4DET0, Q4DF18, Q4DF20, Q4DF36, Q4DF59, Q4DFA8, Q4DFB8, Q4DFD2, Q4DFE2, Q4DFF8, Q4DFG3, Q4DFI8, Q4DFJ5, Q4DFL2, Q4DFM2, Q4DFP0, Q4DFP8, Q4DFR9, Q4DFY0, Q4DG00, Q4DG03, Q4DG06, Q4DG22, Q4DG40, Q4DG45, Q4DG60, Q4DG63, Q4DG77, Q4DG96, Q4DGA2, Q4DGE9, Q4DGL9, Q4DGP8, Q4DGP9, Q4DGT9, Q4DGU2, Q4DGW6, Q4DH63, Q4DH94, Q4DHB2, Q4DHC6, Q4DHD3, Q4DHD9, Q4DHG7, Q4DHI7, Q4DHL4, Q4DHP0, Q4DHP4, Q4DHP8, Q4DHS8, Q4DHY1, Q4DI05, Q4DI68, Q4DI85, Q4DIB5, Q4DIB9, Q4DIF6, Q4DIG2, Q4DIJ8, Q4DIR3, Q4DIR4, Q4DIX2, Q4DIX3, Q4DJ19, Q4DJ30, Q4DJ36, Q4DJ40, Q4DJ42, Q4DJ49, Q4DJ96, Q4DJA1, Q4DJC9, Q4DJD0, Q4DJF1, Q4DJN0, Q4DJN8, Q4DJQ5, Q4DJQ7, Q4DJR7, Q4DJT8, Q4DJX1, Q4DJZ1, Q4DJZ9, Q4DK31, Q4DK73, Q4DK88, Q4DKG4, Q4DKI5, Q4DKK5, Q4DKQ2, Q4DKT2, Q4DKU5, Q4DKU9, Q4DKX0, Q4DKY2, Q4DKY7, Q4DKY8, Q4DKZ4, Q4DL24, Q4DL81, Q4DL82, Q4DLB9, Q4DLH1, Q4DLI2, Q4DLL1, Q4DLM5, Q4DLN7, Q4DLU4, Q4DLY6, Q4DLZ0, Q4DM53, Q4DM59, Q4DM81, Q4DM82, Q4DM83, Q4DME7, Q4DME9, Q4DMG9, Q4DMH1, Q4DMH3, Q4DMK9, Q4DMU8, Q4DMU9, Q4DMV1, Q4DMW3, Q4DMX9, Q4DN30, Q4DN34, Q4DNB9, Q4DNL0, Q4DNM4, Q4DNR3, Q4DNU7, Q4DP31, Q4DP48, Q4DPB6, Q4DPC8, Q4DPE4, Q4DPH7, Q4DPH9, Q4DPI6, Q4DPL8, Q4DPM2, Q4DPP9, Q4DPQ9, Q4DPR3, Q4DPS5, Q4DPS6, Q4DPV6, Q4DPV9, Q4DPX8, Q4DPZ5, Q4DQ27, Q4DQ35, Q4DQ37, Q4DQ63, Q4DQ86, Q4DQJ3, Q4DQQ7, Q4DQS9, Q4DQT6, Q4DQV3, Q4DQZ1, Q4DR16, Q4DR33, Q4DR82, Q4DRB5, Q4DRE9, Q4DRF1, Q4DRF5, Q4DRJ9, Q4DRK8, Q4DRL1, Q4DRN5, Q4DRW8, Q4DS83, Q4DSA0, Q4DSE6, Q4DSF3, Q4DSI2, Q4DSI7, Q4DSJ1, Q4DSL1, Q4DSM6, Q4DSP6, Q4DSP9, Q4DST2, Q4DST7, Q4DSU6, Q4DSW2, Q4DSW8, Q4DSZ1, Q4DSZ8, Q4DT66, Q4DT70, Q4DT78, Q4DTA0, Q4DTD7, Q4DTE0, Q4DTE6, Q4DTE8, Q4DTE9, Q4DTI1, Q4DTI4, Q4DTJ6, Q4DTQ1, Q4DTR0, Q4DTR8, Q4DTU3, Q4DTU8, Q4DTW1, Q4DTX5, Q4DU38, Q4DU59, Q4DU60, Q4DU83, Q4DU88, Q4DUB8, Q4DUD1, Q4DUD6, Q4DUF6, Q4DUG1, Q4DUH1, Q4DUI3, Q4DUK6, Q4DUM4, Q4DUP6, Q4DUP9, Q4DUR6, Q4DUT9, Q4DUU1, Q4DUW5, Q4DUX1, Q4DUX9, Q4DV13, Q4DV14, Q4DV61, Q4DV75, Q4DV93, Q4DVF8, Q4DVG6, Q4DVM9, Q4DVV0, Q4DW27, Q4DW33, Q4DW38, Q4DW49, Q4DW59, Q4DW67, Q4DW83, Q4DWB5, Q4DWC3, Q4DWC5, Q4DWD1, Q4DWI0, Q4DWK5, Q4DWN4, Q4DWS5, Q4DWX5, Q4DWX7, Q4DWX8, Q4DWY3, Q4DX01, Q4DX64, Q4DX67, Q4DX76, Q4DX81, Q4DXC5, Q4DXK1, Q4DXK6, Q4DXK7, Q4DXR1, Q4DXW6, Q4DXW9, Q4DXX0, Q4DXX2, Q4DXX9, Q4DXY6, Q4DY15, Q4DY42, Q4DY45, Q4DY53, Q4DY80, Q4DYE0, Q4DYG1, Q4DYH1, Q4DYH2, Q4DYH7, Q4DYH8, Q4DYL9, Q4DYP1, Q4DYP5, Q4DYQ9, Q4DYS1, Q4DYS2, Q4DYS3, Q4DYW4, Q4DZ02, Q4DZ63, Q4DZ97, Q4DZ98, Q4DZ99, Q4DZB0, Q4DZC9, Q4DZF5, Q4DZJ8, Q4DZK7, Q4DZM2, Q4DZM9, Q4DZN7, RL18, Q4DZP3, Q4DZQ8, Q4DZR2, Q4DZR8, Q4DZT1, Q4DZU7, Q4DZW1, Q4E025, Q4E085, Q4E087, Q4E088, Q4E093, IF61, Q4E0C2, Q4E0D4, Q4E0F9, Q4E0G0, Q4E0G8, Q4E0G9, Q4E0K0, Q4E0L0, Q4E0M2, Q4E0P7, Q4E0P9, Q4E0Q6, Q4E0R0, Q4E0R4, Q4E0T1, Q4E0Y0, Q4E0Y2, Q4E121, Q4E133, IF4A, Q4E1B7, Q4E1D4, Q4E1M3, Q4E1N1, Q4E1R5, Q4E1X0, Q4E1X1, Q4E256, Q4E2D6, Q4E2E5, Q4E2I6, Q4E2J8, Q4E2Q9, Q4E2T9, Q4E2U5, Q4E2V9, Q4E2Y1, Q4E322, Q4E333, Q4E340, Q4E342, Q4E396, Q4E3F7, Q4E3H4, Q4E3J6, Q4E3K5, Q4E3L2, Q4E3M6, Q4E3N3, Q4E3P1, Q4E3W1, Q4E3Y5, Q4E4E9, Q4E4L7, Q4E4N4, Q4E4N6, Q4E4N8, Q4E4P6, Q4E4Q8, Q4E4R0, Q4E4S2, Q4E4T3, Q4E4T4, Q4E4V2, Q4E4W2, Q4E544, Q4E581, Q4E585, Q4E5A0, Q4E5D6, Q4E5G9, Q4E5H0, Q4E5I4, Q4E5Z1, Q4E602, Q4E617, Q4E642, Q4E650, Q4E663, Q58XP3, Q5EFD2, Q670S5, Q6B9P3, Q6BCB3, Q6QR20, Q6QT30, Q6WAT4, Q6XD84, Q6Y8Q6, Q6ZXB9, Q7YUF0, Q7YZX6, Q7Z1X0, Q869B2, Q8I6L9, Q8I728, Q8MZQ5, Q8STF3, Q8T7V6, Q8T8E0, Q8T8E2, Q8T9X5, Q8WQR2, Q8WR03, Q8WTN6, Q94798, Q95WZ9, Q9GN79, Q9GU99, Q9NG30, Q9U664, Q9U681, Q9XY64, V5A3P8, V5A4R3, V5AIW7, V5AJF7,